Abstract A nucleotidyltransferase associated with the chromatinrich fraction of sugar beet tissue has been isolated. The product of the enzyme-catalyzed reaction is a ribohomopolymer. The reaction requires Mg2+ or Mn2+ for activity. In the presence of Mg2+ only CTP is utilized as substrate, however, in the presence of Mn2+, ATP, GTP, and UTP are also utilized but much less than CTP. When Mg2+ is present at optimal concentration (37.5 mm) the addition of Mn2+ to the reaction inhibits CMP incorporation. Incorporation of CMP is inhibited by DNase I, trypsin, other nucleoside triphosphates (ATP, GTP, and UTP), and inorganic pyrophosphate, but not by pancreatic RNase and actinomycin D. It is concluded that the enzyme activity can be classified as a CTP-polymerase.
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